7LTW

Crystal structure of the mouse Kirrel2 D1 homodimer

7LTW の概要

• エントリーDOI: 10.2210/pdb7ltw/pdb
• 分子名称: Kin of IRRE-like protein 2, SODIUM ION (3 entities in total)
• 機能のキーワード: immunoglobulin superfamily, cell surface receptor, nervous system, cell adhesion
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23972.67

構造登録者

Roman, C.A.,Pak, J.S.,Wang, J.,Ozkan, E. (登録日: 2021-02-20, 公開日: 2021-11-24, 最終更新日: 2024-10-23)

主引用文献

Wang, J.,Vaddadi, N.,Pak, J.S.,Park, Y.,Quilez, S.,Roman, C.A.,Dumontier, E.,Thornton, J.W.,Cloutier, J.F.,Ozkan, E.
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors.
Cell Rep, 37:109940-109940, 2021

PubMed Abstract: Projections from sensory neurons of olfactory systems coalesce into glomeruli in the brain. The Kirrel receptors are believed to homodimerize via their ectodomains and help separate sensory neuron axons into Kirrel2- or Kirrel3-expressing glomeruli. Here, we present the crystal structures of homodimeric Kirrel receptors and show that the closely related Kirrel2 and Kirrel3 have evolved specific sets of polar and hydrophobic interactions, respectively, disallowing heterodimerization while preserving homodimerization, likely resulting in proper segregation and coalescence of Kirrel-expressing axons into glomeruli. We show that the dimerization interface at the N-terminal immunoglobulin (IG) domains is necessary and sufficient to create homodimers and fail to find evidence for a secondary interaction site in Kirrel ectodomains. Furthermore, we show that abolishing dimerization of Kirrel3 in vivo leads to improper formation of glomeruli in the mouse accessory olfactory bulb as observed in Kirrel3 animals. Our results provide evidence for Kirrel3 homodimerization controlling axonal coalescence.

PubMed: 34731636
DOI: 10.1016/j.celrep.2021.109940

実験手法

X-RAY DIFFRACTION (1.8 Å)